
Enzyme
Les inhibiteurs d'enzymes sont des molécules qui se lient aux enzymes et diminuent leur activité. Ces inhibiteurs sont largement utilisés en recherche pour étudier la cinétique enzymatique, la régulation et le rôle spécifique des enzymes dans les voies métaboliques. Les inhibiteurs d'enzymes sont également cruciaux dans le développement de médicaments, car de nombreux agents thérapeutiques agissent en inhibant les enzymes impliquées dans les processus pathologiques. En ciblant les enzymes, ces inhibiteurs peuvent moduler les voies biochimiques et offrir des traitements potentiels pour diverses maladies. Chez CymitQuimica, nous offrons une sélection complète d'inhibiteurs d'enzymes de haute qualité pour soutenir vos recherches en biochimie, pharmacologie et découverte de médicaments.
Sous-catégories appartenant à la catégorie "Enzyme"
- Anhydrase carbonique(195 produits)
- Hydroxylase(35 produits)
- MPO(2 produits)
- Réductase(50 produits)
- Tyrosinase(71 produits)
3616 produits trouvés pour "Enzyme"
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Malate dehydrogenase,buffered aqueous glycerol solution, 600-1000 units/mg protein (biuret)
CAS :Malic dehydrogenase is a mitochondrial isozyme and an important catalyst in the tricarboxylic acid cycle. The enzyme catalyzes the following reaction: Oxaloacetate + β-NADH → L-Malate + β-NADOne unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25 °C.Degré de pureté :Min. 95%Ribonuclease A
CAS :<p>Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.</p>Diaphorase (from Clostridium kluyveri)
CAS :Diaphorase (lipoyl dehydrogenase, EC 1.8.1.4) is an NAD+/NADH-dependent oxidoreductase. One unit of diaphorase will convert 1.0 μmole NADH into NAD+ the presence of substrate at pH 7.5 and 25 °C.Degré de pureté :Min. 95%Chitinase
CAS :Chitinase (systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase, EC 3.2.1.14) is a hydrolase that breaks down glycosidic bonds in chitin. One unit of chitinase will yield 1.0 mg of N-acetyl-D-glucosamine from chitin per hour at pH 6.0 and 25 °C.Formule :C17H16N8ZnDegré de pureté :Min. 95%Masse moléculaire :397.74 g/molβ-Glucuronidase from Helix pomatia - Type H-2, aqueous solution, ≥85,000 units/mL
CAS :β-Glucuronidase (EC 3.2.1.31) is an enzyme that hydrolyzes glucuronides. It can also be used to cleave benzodiazepine and steroid conjugates. One unit of β-Glucuronidase will hydrolyze a chromogenic substrate mimic 4-nitrophenyl-β-D-glucuronide to produce 1.0 μmole of 4-nitrophenol per minute at pH 5.0 and 37 °C.Degré de pureté :Min. 95%Couleur et forme :Clear LiquidC. rugosa Lipase 03, CRL 3 from Candida rugosa - ELCR03
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The Lipase 03 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.C. rugosa Lipase 01, CRL 1 from Candida rugosa - ELCR01
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The Lipase 01 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Carboxypeptidase Y, from S. cerevisiae, recombinant, lyophilized - ECPY001
CAS :Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product. Carboxypeptidase Y has been obtained from yeast S. cerevisiae, has a broad substrate specificity and can therefore be used in sequence analysis of proteins. Carboxypeptidase Y has a temperature optimum in the 20 – 30 °C range and pH optimum between pH 6 and 7.Acid phosphatase
CAS :One unit will hydrolyse 1.0μmol of 4-nitrophenyl phosphate per minute at 37°C and pH 4.8. Substrate for enzyme analysis is the 4-nitrophenyl phosphate disodium hexahydrate (EN08508).Formule :C6H10O2Degré de pureté :Min. 95%Masse moléculaire :114.14 g/molLipoxidase
CAS :Lipoxidase is an enzyme, which is typically sourced from various plant tissues, animals, and some microorganisms. It functions by catalyzing the oxidation of polyunsaturated fatty acids in the presence of oxygen. This enzymatic action results in the formation of lipid hydroperoxides, which are key intermediates in various biochemical pathways, including those involved in cell signaling and the modulation of gene expression.Degré de pureté :Min. 95%EUCODIS® CalB02 IA, engineered variant of Candida antarctica Lipase B, immobilized by adsorption on hydrophobic carrier - ELCB02IA
<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The CalB02 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>Chloroperoxidase, aqueous suspension
CAS :<p>Chloroperoxidase (also known as chloride peroxidase, systemic name chloride:hydrogen-peroxide oxidoreductase, EC 1.11.1.10) is an enzyme that catalyzes chlorination of organic compounds. Overall reaction is the following:R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O; reaction intermediate is hypochlorous acid (HOCl). One unit of chloroperoxidase will convert 1.0 μmole of substrate per minute.</p>Couleur et forme :PowderProteinase, Bacillus subtilis, sutilain
CAS :Proteinase, Bacillus subtilis, sutilain is a proteolytic enzyme, which is derived from the bacterium Bacillus subtilis. This enzyme exhibits a serine-type mechanism of action, characterized by its ability to cleave peptide bonds in proteins efficiently. It catalyzes the hydrolysis of proteins into peptides and amino acids, facilitating the breakdown of complex proteins into simpler, soluble forms.Degré de pureté :Min. 95%Couleur et forme :PowderProtease from Streptomyces griseus
CAS :<p>Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.</p>Degré de pureté :Min. 95%Couleur et forme :Powderα Amylase enzyme
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Human pancreatic Alpha Amylase is supplied as clear, colorless to light yellow liquid solution at ≥400U/mL, specific activity ≥100 U/mg protein.Store at 2-8 °C on arrival.Degré de pureté :Min. 95%Ribonuclease T1 from aspergillus oryzae
CAS :Ribonuclease T1 is an endonuclease enzyme, which is derived from the fungus Aspergillus oryzae. It specifically cleaves single-stranded RNA at the 3' end of guanosine residues, which involves hydrolyzing the phosphodiester bond to produce 3′-phosphomononucleotides and 5′-hydroxylated oligonucleotides. This enzyme’s high specificity and catalytic efficiency make it valuable for various applications.Degré de pureté :Min. 95%Transglutaminase from guinea pig liver
CAS :Transglutaminase (2.3.2.13) is an enzyme that catalyzes formation of isopeptide bonds between the γ-carboxamide groups ( -(C=O)NH2 ) of glutamine side chains and amino groups. The donor of the amino group is usually (but not always) an ε-amino group ( -NH2 ) of lysine residue. The reaction also releases ammonia: Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3One unit of transglutaminase will catalyze the formation of 1.0 μmole transglutamination product per min at pH 6.0 and 37 °C.Degré de pureté :Min. 95%Amylase protein
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, ptyalin; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Human salivary Alpha Amylase is supplied as clear, colorless liquid solution at ≥2000U/mL, specific activity ≥200 U/mg protein. Store at -20°C on arrival.Degré de pureté :Min. 95%Cathepsin B from human placenta
CAS :<p>Cathepsin B is a lysosomal proteolytic enzyme of the cysteine protease family. It is present in all mammalian cells. It is essential for the intracellular protein turnover. Cathepsin B may be a useful tool in Alzheimer′s research, as it may have a role in the natural defense against the disease.</p>Degré de pureté :Min. 95%Cellulose catalase
<p>Cellulose catalase is an enzyme-based product, designed specifically to act as a catalyst in the oxidative processes associated with cellulose applications. It is derived from a microbial source, where bacilli or fungi are employed to produce robust catalase enzymes in a fermentation process. The mode of action involves the catalase enzyme’s ability to facilitate the decomposition of hydrogen peroxide into water and oxygen, thereby reducing oxidative damage during cellulose processing.</p>
